7a43-pdb | HEADER HYDROLASE 19-AUG-20 7A43
TITLE FLUOROACETATE DEHALOGENASE MEASURED BY SERIAL FEMTOSECOND
TITLE 2 CRYSTALLOGRAPHY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 1076;
SOURCE 4 GENE: RPA1163;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DEHALOGENASE, SERIAL FEMTOSECOND CRYSTALLOGRAPHY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.MEHRABI,E.C.SCHULZ,R.BUECKER
REVDAT 1 07-APR-21 7A43 0
JRNL AUTH P.MEHRABI,R.BUCKER,G.BOURENKOV,H.M.GINN,D.VON STETTEN,
JRNL AUTH 2 H.M.MULLER-WERKMEISTER,A.KUO,T.MORIZUMI,B.T.EGER,W.L.OU,
JRNL AUTH 3 S.OGHBAEY,A.SARRACINI,J.E.BESAW,O.PARE-LABROSSE,S.MEIER,
JRNL AUTH 4 H.SCHIKORA,F.TELLKAMP,A.MARX,D.A.SHERRELL,D.AXFORD,R.L.OWEN,
JRNL AUTH 5 O.P.ERNST,E.F.PAI,E.C.SCHULZ,R.J.D.MILLER
JRNL TITL SERIAL FEMTOSECOND AND SERIAL SYNCHROTRON CRYSTALLOGRAPHY
JRNL TITL 2 CAN YIELD DATA OF EQUIVALENT QUALITY: A SYSTEMATIC
JRNL TITL 3 COMPARISON.
JRNL REF SCI ADV V. 7 2021
JRNL REFN ESSN 2375-2548
JRNL PMID 33731353
JRNL DOI 10.1126/SCIADV.ABF1380
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18_3855
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 53205
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.450
REMARK 3 FREE R VALUE TEST SET COUNT : 1838
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.0800 - 4.1100 1.00 4155 150 0.1526 0.1660
REMARK 3 2 4.1100 - 3.2700 1.00 4091 148 0.1420 0.1722
REMARK 3 3 3.2600 - 2.8500 1.00 4071 147 0.1622 0.1941
REMARK 3 4 2.8500 - 2.5900 0.99 4049 146 0.1683 0.1906
REMARK 3 5 2.5900 - 2.4100 0.99 4058 141 0.1623 0.2097
REMARK 3 6 2.4100 - 2.2600 0.99 4042 139 0.1560 0.1924
REMARK 3 7 2.2600 - 2.1500 0.99 4005 141 0.1558 0.1973
REMARK 3 8 2.1500 - 2.0600 0.98 3987 136 0.1672 0.2172
REMARK 3 9 2.0600 - 1.9800 0.97 3917 142 0.1713 0.2109
REMARK 3 10 1.9800 - 1.9100 0.96 3867 146 0.1748 0.2633
REMARK 3 11 1.9100 - 1.8500 0.94 3844 143 0.1833 0.2630
REMARK 3 12 1.8500 - 1.8000 0.91 3693 129 0.2079 0.2428
REMARK 3 13 1.8000 - 1.7500 0.89 3588 130 0.2250 0.2678
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.177
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.231
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 4902
REMARK 3 ANGLE : 1.252 6685
REMARK 3 CHIRALITY : 0.067 685
REMARK 3 PLANARITY : 0.009 881
REMARK 3 DIHEDRAL : 36.454 665
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7A43 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1292110817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER
REMARK 200 BEAMLINE : BL3
REMARK 200 X-RAY GENERATOR MODEL : SACLA BEAMLINE BL3
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.22
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MPCCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54828
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 33.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 101.9
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3R3U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20 % (W/V)) PEG3350, 200 MM CACL2,
REMARK 280 AND 100 MM TRIS-HCL PH 8.5, BATCH MODE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.95000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 301
REMARK 465 PRO A 302
REMARK 465 GLY A 303
REMARK 465 SER A 304
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 ALA B 300
REMARK 465 ALA B 301
REMARK 465 PRO B 302
REMARK 465 GLY B 303
REMARK 465 SER B 304
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 3 CG OD1 OD2
REMARK 470 ARG A 296 CG CD NE CZ NH1 NH2
REMARK 470 THR B 259 OG1 CG2
REMARK 470 ARG B 296 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 556 O HOH A 581 2.10
REMARK 500 O HOH A 627 O HOH A 631 2.18
REMARK 500 O HOH A 556 O HOH B 561 2.18
REMARK 500 O HOH A 580 O HOH A 629 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 41 64.52 -103.13
REMARK 500 ASP A 110 -128.84 60.32
REMARK 500 SER A 123 56.06 -144.69
REMARK 500 ILE A 153 50.84 -115.66
REMARK 500 ASP A 173 72.52 -157.42
REMARK 500 TYR A 224 -97.90 -121.84
REMARK 500 PRO B 41 66.76 -105.08
REMARK 500 ASP B 110 -129.87 57.46
REMARK 500 SER B 123 58.33 -141.52
REMARK 500 ILE B 153 51.05 -112.67
REMARK 500 ASP B 173 74.17 -162.34
REMARK 500 TYR B 224 -97.38 -119.95
REMARK 500 ALA B 286 59.78 -146.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
DBREF 7A43 A 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
DBREF 7A43 B 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
SEQADV 7A43 GLY A -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 7A43 HIS A 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 7A43 GLY A 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 7A43 SER A 304 UNP Q6NAM1 EXPRESSION TAG
SEQADV 7A43 GLY B -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 7A43 HIS B 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 7A43 GLY B 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 7A43 SER B 304 UNP Q6NAM1 EXPRESSION TAG
SEQRES 1 A 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 A 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 A 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 A 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 A 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 A 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 A 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 A 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 A 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 A 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 A 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 A 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 A 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 A 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 A 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 A 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 A 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 A 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 A 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 A 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 A 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 A 306 GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU
SEQRES 23 A 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 A 306 PHE SER ALA ALA PRO GLY SER
SEQRES 1 B 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 B 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 B 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 B 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 B 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 B 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 B 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 B 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 B 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 B 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 B 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 B 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 B 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 B 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 B 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 B 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 B 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 B 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 B 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 B 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 B 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 B 306 GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU
SEQRES 23 B 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 B 306 PHE SER ALA ALA PRO GLY SER
HET CL A 401 1
HET CL B 401 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *306(H2 O)
HELIX 1 AA1 THR A 43 HIS A 48 5 6
HELIX 2 AA2 VAL A 50 GLU A 56 1 7
HELIX 3 AA3 HIS A 80 TYR A 83 5 4
HELIX 4 AA4 THR A 84 LEU A 99 1 16
HELIX 5 AA5 ASP A 110 SER A 123 1 14
HELIX 6 AA6 PRO A 137 ARG A 144 1 8
HELIX 7 AA7 ASN A 146 ILE A 153 1 8
HELIX 8 AA8 ILE A 153 LEU A 159 1 7
HELIX 9 AA9 PRO A 164 GLY A 171 1 8
HELIX 10 AB1 ASP A 173 TRP A 185 1 13
HELIX 11 AB2 ASP A 195 ALA A 207 1 13
HELIX 12 AB3 ASP A 208 TYR A 224 1 17
HELIX 13 AB4 TYR A 224 GLY A 237 1 14
HELIX 14 AB5 THR A 259 ALA A 268 1 10
HELIX 15 AB6 PHE A 281 ALA A 286 1 6
HELIX 16 AB7 ALA A 286 ALA A 300 1 15
HELIX 17 AB8 THR B 43 HIS B 48 5 6
HELIX 18 AB9 VAL B 50 ALA B 55 1 6
HELIX 19 AC1 HIS B 80 TYR B 83 5 4
HELIX 20 AC2 THR B 84 LEU B 99 1 16
HELIX 21 AC3 ASP B 110 SER B 123 1 14
HELIX 22 AC4 PRO B 137 ARG B 144 1 8
HELIX 23 AC5 ASN B 146 ILE B 153 1 8
HELIX 24 AC6 TYR B 154 LEU B 159 1 6
HELIX 25 AC7 PRO B 164 GLY B 171 1 8
HELIX 26 AC8 ASP B 173 TRP B 185 1 13
HELIX 27 AC9 ASP B 195 ASP B 208 1 14
HELIX 28 AD1 ASP B 208 TYR B 224 1 17
HELIX 29 AD2 TYR B 224 GLY B 237 1 14
HELIX 30 AD3 ILE B 253 ALA B 258 1 6
HELIX 31 AD4 THR B 259 LYS B 266 1 8
HELIX 32 AD5 PHE B 281 ALA B 286 1 6
HELIX 33 AD6 ALA B 286 SER B 299 1 14
SHEET 1 AA1 8 GLY A 12 ILE A 16 0
SHEET 2 AA1 8 ILE A 23 GLY A 29 -1 O ILE A 23 N ILE A 16
SHEET 3 AA1 8 LYS A 59 ALA A 63 -1 O VAL A 62 N ARG A 26
SHEET 4 AA1 8 PRO A 33 LEU A 37 1 N LEU A 34 O ILE A 61
SHEET 5 AA1 8 PHE A 104 HIS A 109 1 O ALA A 105 N LEU A 35
SHEET 6 AA1 8 LEU A 127 LEU A 133 1 O ALA A 131 N LEU A 106
SHEET 7 AA1 8 MET A 244 GLY A 249 1 O LEU A 247 N VAL A 132
SHEET 8 AA1 8 VAL A 271 ILE A 276 1 O GLN A 272 N ALA A 246
SHEET 1 AA2 8 GLY B 12 ILE B 16 0
SHEET 2 AA2 8 ILE B 23 GLY B 28 -1 O VAL B 27 N GLY B 12
SHEET 3 AA2 8 LYS B 59 ALA B 63 -1 O VAL B 62 N ARG B 26
SHEET 4 AA2 8 PRO B 33 LEU B 37 1 N LEU B 34 O ILE B 61
SHEET 5 AA2 8 PHE B 104 HIS B 109 1 O ALA B 105 N LEU B 35
SHEET 6 AA2 8 LEU B 127 LEU B 133 1 O ALA B 131 N LEU B 106
SHEET 7 AA2 8 MET B 244 GLY B 249 1 O LEU B 245 N VAL B 132
SHEET 8 AA2 8 VAL B 271 ILE B 276 1 O ILE B 276 N TRP B 248
CISPEP 1 PHE A 40 PRO A 41 0 -1.77
CISPEP 2 ALA A 163 PRO A 164 0 2.37
CISPEP 3 PHE B 40 PRO B 41 0 -1.68
CISPEP 4 ALA B 163 PRO B 164 0 0.16
SITE 1 AC1 4 ASP A 110 ARG A 114 HOH A 513 HOH A 642
SITE 1 AC2 3 ASP B 110 ARG B 114 HOH B 501
CRYST1 41.900 79.900 84.800 90.00 103.40 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023866 0.000000 0.005686 0.00000
SCALE2 0.000000 0.012516 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012122 0.00000
TER 2395 ALA A 300
TER 4745 SER B 299
MASTER 282 0 2 33 16 0 2 6 4998 2 0 48
END
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